Protein conformations have been investigated by calculations which include either short and medium range or long range interactions. These include 1) predictions of regular secondary regions, with a method which does not depend on reported X-ray crystal forms, and 2) investigations of folding pathways of proteins with a simple model in which the native conformation is favored. In the first case, it it found that, similar to other secondary conformation prediction methods, only about 60% of the residues are favored in their native conformation, if only short and medium range interactions are included. The implication is that long range interactions modify intrinsically preferred conformations of significant numbers of residues. From the second calculations which include long range interactions, definite folding pathways are obtained for pancreatic trypsin inhibitor, myoglobin, ribonuclease, concanavalin A, and lysozyme. The activated state for the folding-unfolding process is found to correspond to the appearance of long range interactions. In all cases only one or two regions of growing nuclei are observed.